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Journal article

The startle disease mutation E103K impairs activation of human homomeric α1 glycine receptors by disrupting an intersubunit salt bridge across the agonist binding site.

Abstract:

Glycine receptors (GlyR) belong to the pentameric ligand-gated ion channel (pLGIC) superfamily and mediate fast inhibitory transmission in the vertebrate CNS. Disruption of glycinergic transmission by inherited mutations produces startle disease in man. Many startle mutations are in GlyRs and provide useful clues to the function of the channel domains. E103K is one of few startle mutations found in the extracellular agonist binding site of the channel, in loop A of the principal side of the s...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1074/jbc.M116.767616

Authors


Hurdiss, E More by this author
Erotocritou, M More by this author
Greiner, T More by this author
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University College London More from this funder
Oxford Wolfson Marriott Biochemistry Graduate Scholarship More from this funder
German Academic Scholarship Foundation More from this funder
Publisher:
American Society for Biochemistry and Molecular Biology On Publisher's website
Journal:
Journal of Biological Chemistry Journal website
Volume:
292
Issue:
12
Pages:
5031-5042
Publication date:
2017-02-05
Acceptance date:
2017-01-25
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Pubs id:
pubs:679548
URN:
uri:09908eaa-194f-4bbd-8b5d-fd87985e139f
UUID:
uuid:09908eaa-194f-4bbd-8b5d-fd87985e139f
Local pid:
pubs:679548

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